9PWQ
Cryo-EM structure of receptor tyrosine kinase ROS1 extracellular domain in complex with NELL2
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtpgsFmCiC |
| Chain | Residue | Details |
| B | CYS457-CYS468 | |
| B | CYS572-CYS583 | |
| B | CYS619-CYS630 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CaCpqGftGPsC |
| Chain | Residue | Details |
| B | CYS541-CYS552 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. CiCktGYiriddys.C |
| Chain | Residue | Details |
| B | CYS466-CYS480 | |
| B | CYS508-CYS521 | |
| B | CYS541-CYS552 | |
| B | CYS663-CYS677 |
| site_id | PS01187 |
| Number of Residues | 27 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECaegrhy........Crentm..CvNtpgsFmC |
| Chain | Residue | Details |
| B | ASP440-CYS466 | |
| B | ASP555-CYS581 | |
| B | ASP602-CYS628 |
| site_id | PS01208 |
| Number of Residues | 40 |
| Details | VWFC_1 VWFC domain signature. Ckn.CTClngtiq........CetliCpnpd......Cplksalayvdgk....CCke..C |
| Chain | Residue | Details |
| B | CYS291-CYS330 | |
| B | CYS719-CYS755 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 95 |
| Details | Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 88 |
| Details | Domain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 100 |
| Details | Domain: {"description":"Fibronectin type-III 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 95 |
| Details | Domain: {"description":"Fibronectin type-III 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 107 |
| Details | Domain: {"description":"Fibronectin type-III 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 107 |
| Details | Domain: {"description":"Fibronectin type-III 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 99 |
| Details | Domain: {"description":"Fibronectin type-III 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 7 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 59 |
| Details | Domain: {"description":"VWFC 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00220","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 42 |
| Details | Domain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 41 |
| Details | Domain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
